| Analysis | rpsblast_cdd | Start | 194 |
| End | 318 | Strand | + |
| Length | 125 | Note | Gaps:12 |
| Hit Coverage | 34.97 | Hit Length | 346 |
| Hit Pident | 32.23 | E Val | 1e-11 |
| Hit Description | cd07475 Peptidases_S8_C5a_Peptidase Peptidase S8 family domain in Streptococcal C5a peptidases. Streptococcal C5a peptidase (SCP) is a highly specific protease and adhesin/invasin. The subtilisin-like protease domain is located at the N-terminus and contains a protease-associated domain inserted into a loop. There are three fibronectin type III (Fn) domains at the C-terminus. SCP binds to integrins with the help of Arg-Gly-Asp motifs which are thought to stabilize conformational changes required for substrate binding. Peptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular some function at extreme temperatures and pH values. | Hit Pcons | 10.74 |
| Name | Qrob_P0036570.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0036570.2 | Quercus robur | 0.0 | egn | (M=44) 3.4.14.10 - Tripeptidyl-peptidase II. | EC:3.4.14.10 | validated |
Powered by
